Heme Oxygenase 2 Antibody
Purified Rabbit Polyclonal Antibody (Pab)
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Application
| WB |
|---|---|
| Primary Accession | P30519 |
| Reactivity | Human, Mouse |
| Host | Rabbit |
| Clonality | Polyclonal |
| Calculated MW | 36033 Da |
| Gene ID | 3163 |
|---|---|
| Other Names | Heme oxygenase 2, HO-2, HMOX2, HO2 |
| Target/Specificity | KLH-conjugated synthetic peptide encompassing a sequence within the N-term region of human Heme Oxygenase 2. The exact sequence is proprietary. |
| Dilution | WB~~1:1000 |
| Format | 0.01M PBS, pH 7.2, 0.09% (W/V) Sodium azide, Glycerol 50% |
| Storage | Store at -20 °C.Stable for 12 months from date of receipt |
| Name | HMOX2 |
|---|---|
| Synonyms | HO2 |
| Function | [Heme oxygenase 2]: Catalyzes the oxidative cleavage of heme at the alpha-methene bridge carbon, released as carbon monoxide (CO), to generate biliverdin IXalpha, while releasing the central heme iron chelate as ferrous iron. |
| Cellular Location | Microsome membrane; Single-pass type IV membrane protein; Cytoplasmic side {ECO:0000250|UniProtKB:P09601}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P09601}; Single-pass type IV membrane protein; Cytoplasmic side {ECO:0000250|UniProtKB:P09601} |
For Research Use Only. Not For Use In Diagnostic Procedures.
Provided below are standard protocols that you may find useful for product applications.
BACKGROUND
Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. Heme oxygenase 2 could be implicated in the production of carbon monoxide in brain where it could act as a neurotransmitter.
REFERENCES
Ishikawa K.,et al.J. Biol. Chem. 270:6345-6350(1995).
McCoubrey W.K. Jr.,et al.Arch. Biochem. Biophys. 295:13-20(1992).
Kalnine N.,et al.Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
Martin J.,et al.Nature 432:988-994(2004).
Mural R.J.,et al.Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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